The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Brevican distinctively assembles extracellular components at the large diameter nodes of Ranvier in the CNS
Abstract
Brevican is known to be an abundant extracellular matrix component in the adult brain and a structural constituent of perineuronal nets. We herein show that brevican, tenascin‐R (TN‐R) and phosphacan are present at the nodes of Ranvier on myelinated axons with a particularly large diameter in the central nervous system. A brevican deficiency resulted in a reorganization of the nodal matrices, which was characterized by the shift of TN‐R, and concomitantly phosphacan, from an axonal diameter‐dependent association with nodes to an axonal diameter independent association. Supported by the co‐immunoprecipitation results, these observations indicate that the presence of TN‐R and phosphacan at nodes is normally brevican‐dependent, while in the absence of brevican these molecules can also be recruited by versican V2. The versican V2 and Bral1 distribution was not affected, thus indicating a brevican‐independent role of these two molecules for establishing hyaluronan‐binding matrices at the nodes. Our results revealed that brevican plays a crucial role in determining the specialization of the hyaluronan‐binding nodal matrix assemblies in large diameter nodes.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The HLT model turn out to be a very far-sighted model not only for the PNN molecular organization but also for the perinodal ECM molecular organization (Bekku et al., 2009).”
From The hyaluronan and proteoglycan link proteins: Organizers of the brain extracellular matrix and key molecules for neuronal function and plasticity (2015) · cites this paper as Bekku et al., 2009
In the citing paper
“We thus proposed that the hyaluronan-associated ECM could serve as an”
From The hyaluronan and proteoglycan link proteins: Organizers of the brain extracellular matrix and key molecules for neuronal function and plasticity (2015) · cites this paper as Bekku et al., 2009
In the citing paper
“Brevican and neurocan are also known to localize at the nodes in an axon diameter-dependent manner (Fig. 5; Bekku et al., 2009;Bekku and Oohashi, 2010).”
From The hyaluronan and proteoglycan link proteins: Organizers of the brain extracellular matrix and key molecules for neuronal function and plasticity (2015) · cites this paper as Bekku et al., 2009
In the citing paper
“Of particular note is that the HLT model made from PNN fits to this PM except for the differences that vercican V2 is the most common lectican and aggrecan is absent at the node (Bekku et al., 2009;Dours-Zimmermann et al., 2009).”
From The hyaluronan and proteoglycan link proteins: Organizers of the brain extracellular matrix and key molecules for neuronal function and plasticity (2015) · cites this paper as Bekku et al., 2009
In the citing paper
“The nodes of particularly large diameter have a more elaborate ECM assembly than the nodes of smaller axons, as if the ECM could further speed up axonal velocity by a reduction in the resistance of the extracellular medium (Bekku et al., 2009).”
From The hyaluronan and proteoglycan link proteins: Organizers of the brain extracellular matrix and key molecules for neuronal function and plasticity (2015) · cites this paper as Bekku et al., 2009
Citations
Cites
The local differentiation of myelinated axons at nodes of Ranvier
Poliak, S., & Peles, E. (2003) · Nature reviews. Neuroscience · doi:10.1038/nrn1253 · Cited by 650
Lecticans: organizers of the brain extracellular matrix
Yamaguchi, Y. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000690 · Cited by 642
Polarized Domains of Myelinated Axons
Salzer, J. L. (2003) · Neuron · doi:10.1016/s0896-6273(03)00628-7 · Cited by 416
Carulli, D., Rhodes, K. E., Brown, D. J., Bonnert, T. P., Pollack, S. J., Oliver, K., Strata, P., & Fawcett, J. W. (2006) · Journal of Comparative Neurology · doi:10.1002/cne.20822 · Cited by 341
Aspberg, A., Miura, R., Bourdoulous, S., Shimonaka, M., Heinegård, D., Schachner, M., Ruoslahti, E., & Yamaguchi, Y. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.19.10116 · Cited by 275
Neurofascin assembles a specialized extracellular matrix at the axon initial segment
Hedstrom, K. L., Xu, X., Ogawa, Y., Frischknecht, R., Seidenbecher, C. I., Shrager, P., & Rasband, M. N. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200705119 · Cited by 268
Brakebusch, C., Seidenbecher, C. I., Asztely, F., Rauch, U., Matthies, H., Meyer, H., Krug, M., Böckers, T. M., Zhou, X., Kreutz, M. R., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.21.7417-7427.2002 · Cited by 264
Self-citationWeber, P., Bartsch, U., Rasband, M. N., Czaniera, R., Lang, Y., Bluethmann, H., Margolis, R. U., Levinson, S. R., Shrager, P., Montag, D., et al. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-11-04245.1999 · Cited by 247
Molecular domains of myelinated axons.
Peles, E., & Salzer, J. (2000) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(00)00122-7 · Cited by 242
Neurocan Is Dispensable for Brain Development
Zhou, X.-H., Brakebusch, C., Matthies, H., Oohashi, T., Hirsch, E., Moser, M., Krug, M., Seidenbecher, C. I., Boeckers, T. M., Rauch, U., et al. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.17.5970-5978.2001 · Cited by 206
Self-citation
Research works printed but not linked: 3
- Augustine G. J., 2008, Neuroscience, 52
- Oohashi T., 2007, Neural Proteoglycans, 67
- Scott J. E., 1998, Glycoforum
Cited by
Sorted by citations
The roles of perineuronal nets and the perinodal extracellular matrix in neuronal function
Fawcett, J. W., Oohashi, T., & Pizzorusso, T. (2019) · Nature Reviews Neuroscience · doi:10.1038/s41583-019-0196-3 · Cited by 589
Self-citationExtracellular Matrix: Functions in the Nervous System
Barros, C. S., Franco, S. J., & Muller, U. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005108 · Cited by 506
Crosstalk between glia, extracellular matrix and neurons
Song, I., & Dityatev, A. E. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.03.003 · Cited by 270
Dityatev, A. E., Seidenbecher, C. I., & Schachner, M. (2010) · Trends in Neurosciences · doi:10.1016/j.tins.2010.08.003 · Cited by 235
Faissner, A., Pyka, M., Geissler, M., Sobik, T., Frischknecht, R., Gundelfinger, E. D., & Seidenbecher, C. (2010) · Brain Research Reviews · doi:10.1016/j.brainresrev.2010.01.001 · Cited by 207
Three mechanisms assemble central nervous system nodes of Ranvier
Susuki, K., Chang, K.-J., Zollinger, D. R., Liu, Y., Ogawa, Y., Eshed-Eisenbach, Y., Dours-Zimmermann, M. T., Oses-Prieto, J. A., Burlingame, A. L., Seidenbecher, C. I., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.03.005 · Cited by 186
“Nodal clustering of the ECM molecules phosphacan, tenascin-R, and neurocan (Ncan) depends on the proteoglycan Vcan and/or the proteoglycan Bcan (Figure 2A; Bekku and Oohashi, 2010; Bekku et al., 2009; Dours-Zimmermann et al., 2009).”
BackgroundInfluentialSelf-citationExtracellular matrix abnormalities in schizophrenia
Berretta, S. (2012) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.08.010 · Cited by 179
Hemphill, M. A., Dauth, S., Yu, C. J., Dabiri, B. E., & Parker, K. K. (2015) · Neuron · doi:10.1016/j.neuron.2015.02.041 · Cited by 180
Mechanisms of node of Ranvier assembly
Rasband, M. N., & Peles, E. (2020) · Nature reviews. Neuroscience · doi:10.1038/s41583-020-00406-8 · Cited by 180
Chondroitin sulfate: A key molecule in the brain matrix
Kwok, J. C. F., Warren, P. M., & Fawcett, J. W. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.01.004 · Cited by 138
Mechanisms of sodium channel clustering and its influence on axonal impulse conduction
Freeman, S. A., Desmazières, A., Fricker, D., Lubetzki, C., & Sol‐Foulon, N. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2081-1 · Cited by 148
Pyka, M., Wetzel, C., Aguado, A., Geissler, M., Hatt, H., & Faissner, A. (2011) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2011.07690.x · Cited by 131
Oohashi, T., Edamatsu, M., Bekku, Y., & Carulli, D. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.09.010 · Cited by 131
Self-citationBral1: its role in diffusion barrier formation and conduction velocity in the CNS
Bekku, Y., Vargová, L., Goto, Y., Vorísek, I., Dmytrenko, L., Narasaki, M., Ohtsuka, A., Fässler, R., Ninomiya, Y., Syková, E., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5598-09.2010 · Cited by 123
Self-citationVersican V2 Assembles the Extracellular Matrix Surrounding the Nodes of Ranvier in the CNS
Dours-Zimmermann, M. T., Maurer, K., Rauch, U., Stoffel, W., Fassler, R., & Zimmermann, D. R. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4158-08.2009 · Cited by 123
Self-citationAlfonso‐Loeches, S., Ureña‐Peralta, J. R., Morillo-Bargues, M. J., Gómez‐Pinedo, U., & Guerri, C. (2015) · Neurochemical Research · doi:10.1007/s11064-015-1760-5 · Cited by 122
Nelson, A. D., & Jenkins, P. M. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00136 · Cited by 132
Brevican: A key proteoglycan in the perisynaptic extracellular matrix of the brain
Frischknecht, R., & Seidenbecher, C. I. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.03.022 · Cited by 112
Cell adhesion and matricellular support by astrocytes of the tripartite synapse
Hillen, A. E. J., Burbach, J. P. H., & Hol, E. M. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.02.002 · Cited by 108
Andrews, E. M., Richards, R. J., Yin, F. Q., Viapiano, M. S., & Jakeman, L. B. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.09.008 · Cited by 104
Organization and maintenance of molecular domains in myelinated axons
Buttermore, E. D., Thaxton, C., & Bhat, M. A. (2013) · Journal of Neuroscience Research · doi:10.1002/jnr.23197 · Cited by 96
Krishnaswamy, V. R., Benbenishty, A., Blinder, P., & Sagi, I. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03182-6 · Cited by 96
Glia unglued: How signals from the extracellular matrix regulate the development of myelinating glia
Colognato, H., & Tzvetanova, I. D. (2011) · Developmental Neurobiology · doi:10.1002/dneu.20966 · Cited by 92
Hao, C., Freeman, C. G., Jacobson, G. A., & Small, D. H. (2013) · IUBMB Life · doi:10.1002/iub.1118 · Cited by 99
Nodes of Ranvier during development and repair in the CNS
Lubetzki, C., Sol‐Foulon, N., & Desmazières, A. (2020) · Nature Reviews Neurology · doi:10.1038/s41582-020-0375-x · Cited by 95
Neuro-glial interactions at the nodes of Ranvier: implication in health and diseases
Faivre‐Sarrailh, C., & Devaux, J. J. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00196 · Cited by 90
Acceleration of conduction velocity linked to clustering of nodal components precedes myelination
Freeman, S. A., Desmazières, A., Simonnet, J., Gatta, M., Pfeiffer, F., Aigrot, M. S., Rappeneau, Q., Guerreiro, S., Michel, P. P., Yanagawa, Y., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1419099112 · Cited by 80
Molecular signature of extracellular matrix pathology in schizophrenia
Pantazopoulos, H., Katsel, P., Haroutunian, V. H., Chelini, G., Klengel, T., & Berretta, S. (2020) · European Journal of Neuroscience · doi:10.1111/ejn.15009 · Cited by 81
Inhibitors of myelination: ECM changes, CSPGs and PTPs
Harlow, D. E., & Macklin, W. B. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2013.10.017 · Cited by 79
Role of Chondroitin Sulfate Proteoglycans in Axonal Conduction in Mammalian Spinal Cord
Hunanyan, A. S., García‐Alías, G., Alessi, V., Levine, J. M., Fawcett, J. W., Mendell, L. M., & Arvanian, V. L. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.4659-09.2010 · Cited by 77
Forman, O. P., Penderis, J., Hartley, C., Hayward, L. J., Ricketts, S. L., & Mellersh, C. S. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002462 · Cited by 70
Bekku, Y., Saito, M., Moser, M., Fuchigami, M., Maehara, A., Nakayama, M., Kusachi, S., Ninomiya, Y., & Oohashi, T. (2012) · Journal of Comparative Neurology · doi:10.1002/cne.23009 · Cited by 65
Self-citationInsights into the physiological role of CNS regeneration inhibitors
Baldwin, K. T., & Giger, R. J. (2015) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2015.00023 · Cited by 66
Blosa, M., Sonntag, M., Brückner, G., Jäger, C., Seeger, G., Matthews, R. T., Rübsamen, R., Arendt, T., & Morawski, M. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.10.003 · Cited by 60
Composition, assembly, and maintenance of excitable membrane domains in myelinated axons
Rasband, M. N. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2010.09.010 · Cited by 62
A canine BCAN microdeletion associated with episodic falling syndrome
Gill, J. L., Tsai, K. L., Krey, C., Noorai, R. E., Vanbellinghen, J.-F., GAROSI, L. S., Shelton, G. D., Clark, L. A., & Harvey, R. J. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.07.014 · Cited by 59
Neural ECM molecules in axonal and synaptic homeostatic plasticity
Frischknecht, R., Chang, K.-J., Rasband, M. N., & Seidenbecher, C. I. (2014) · Progress in brain research · doi:10.1016/b978-0-444-63486-3.00004-9 · Cited by 56
Ischemic injury leads to extracellular matrix alterations in retina and optic nerve
Reinhard, J., Renner, M., Wiemann, S., Shakoor, D. A., Stute, G., Dick, H. B., Faissner, A., & Joachim, S. C. (2017) · Scientific Reports · doi:10.1038/srep43470 · Cited by 53
Stevens, S. R., Longley, C. M., Ogawa, Y., Teliska, L. H., Arumanayagam, A. S., Nair, S., Oses-Prieto, J. A., Burlingame, A. L., Cykowski, M. D., Xue, M., et al. (2021) · eLife · doi:10.7554/elife.66491 · Cited by 53
Neural Tissue Homeostasis and Repair Is Regulated via CS and DS Proteoglycan Motifs
Hayes, A. J., & Melrose, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.696640 · Cited by 51
The making of a node: a co-production of neurons and glia
Eshed‐Eisenbach, Y., & Peles, E. (2013) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2013.06.003 · Cited by 50
Glycosaminoglycans and Glycomimetics in the Central Nervous System
Rowlands, D., Sugahara, K., & Kwok, J. C. F. (2015) · Molecules · doi:10.3390/molecules20033527 · Cited by 44
Enzymatic Degradation of Cortical Perineuronal Nets Reverses GABAergic Interneuron Maturation
Willis, A., Pratt, J. A., & MORRIS, B. J. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02772-z · Cited by 38
Neurocan contributes to the molecular heterogeneity of the perinodal ECM
Bekku, Y., & Oohashi, T. (2010) · Archivum histologicum japonicum · doi:10.1679/aohc.73.95 · Cited by 34
Self-citationSaifetiarova, J., Taylor, A. M., & Bhat, M. A. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.2661-16.2017 · Cited by 32
Shabani, Z., Ghadiri, T., Karimipour, M., Sadigh‐Eteghad, S., Mahmoudi, J., Mehrad, H., & Farhoudi, M. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.01.006 · Cited by 28
Ortega, J. A., de Aguiar, G. P. S., Chandravanshi, P., Levy, N., Engel, E., & Álvarez, Z. (2024) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1962 · Cited by 26
Neuron–Oligodendrocyte Communication in Myelination of Cortical GABAergic Cells
Mazuir, E., Fricker, D., & Sol‐Foulon, N. (2021) · Life · doi:10.3390/life11030216 · Cited by 27
Proteoglycans and dental biology: the first review
Listik, E., Gaschler, J. A. M., Matias, M., Feres, M. F. N., Toma, L., & Nahás-Scocate, A. C. R. (2019) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2019.115199 · Cited by 26
ADAMTS‐4 in oligodendrocytes contributes to myelination with an impact on motor function
Pruvost, M., Lépine, M., Leonetti, C., Etard, O., Naveau, M., Agin, V., Docagne, F., Maubert, E., Ali, C., Emery, É., et al. (2017) · Glia · doi:10.1002/glia.23207 · Cited by 30
Fernström, E., Minta, K., Andréasson, U., Sandelius, Å., Wasling, P., Brinkmalm, A., Höglund, K., Blennow, K., Nyman, J., Zetterberg, H., et al. (2018) · Journal of Internal Medicine · doi:10.1111/joim.12763 · Cited by 22
Elbaz, B., Darwish, A., Vardy, M., Isaac, S., Tokars, H. M., Dzhashiashvili, Y., Korshunov, K. S., Prakriya, M., Eden, A., & Popko, B. (2023) · Neuron · doi:10.1016/j.neuron.2023.10.008 · Cited by 21
NG2 Glia: Novel Roles beyond Re-/Myelination
Parolisi, R., & Boda, E. (2018) · Neuroglia · doi:10.3390/neuroglia1010011 · Cited by 23
Wang, Q., Zhou, Q., Zhang, S., Shao, W., Yin, Y., Li, Y., Hou, J., Zhang, X., Guo, Y.-S., Wang, X., et al. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00197 · Cited by 21
Hypoxia-related gene signature for predicting LUAD patients’ prognosis and immune microenvironment
Chen, J., Fu, Y., Hu, J., & He, J. (2022) · Cytokine · doi:10.1016/j.cyto.2022.155820 · Cited by 19
Extracellular matrix proteolysis maintains synapse plasticity during brain development
Nakajo, H., Cao, R., Mula, S. A., McKetney, J., Silva, N. J., Li, K. H., Chalkley, R. J., Randolph, L. K., Shah, M., Rose, I. V. L., et al. (2025) · Nature Neuroscience · doi:10.1038/s41593-025-02153-4 · Cited by 18
Molecular composition of extracellular matrix in the vestibular nuclei of the rat
Rácz, É., Gaál, B., Kecskés, S., & Matesz, C. (2013) · Brain Structure and Function · doi:10.1007/s00429-013-0575-x · Cited by 20
Giamanco, K. A., & Matthews, R. T. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-48457-6_7 · Cited by 17
Accumulation of Neurofascin at Nodes of Ranvier Is Regulated by a Paranodal Switch
Zhang, Y., Yuen, S. K., Peles, E., & Salzer, J. L. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.0830-19.2020 · Cited by 15
Distribution and classification of the extracellular matrix in the olfactory bulb
Hunyadi, A., Gaál, B., Matesz, C., Mészár, Z., Morawski, M., Reimann, K., Lendvai, D., Alpár, A., Wéber, I., & Rácz, É. (2019) · Brain Structure and Function · doi:10.1007/s00429-019-02010-8 · Cited by 14
Popelář, J., GÓMEZ, M. D., Lindovský, J., Rybalko, N., Burianova, J. S., Oohashi, T., & Syka, J. (2017) · Physiological Research · doi:10.33549/physiolres.933605 · Cited by 14
Self-citationO-GalNAc glycans are enriched in neuronal tracts and regulate nodes of Ranvier
Noël, M., Suttapitugsakul, S., Cummings, R. D., & Mealer, R. G. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2418949122 · Cited by 13
Dynamic regulation of the extracellular matrix in reward memory processes: a question of time
Valeri, J., Gisabella, B., & Pantazopoulos, H. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1208974 · Cited by 13
Filho, A. J. M. C., Mottin, M., Lós, D. B., Andrade, C. H., & Macêdo, D. S. (2022) · Biochimie · doi:10.1016/j.biochi.2022.07.015 · Cited by 11
Kecskés, S., Gaál, B., Rácz, É., Birinyi, A., Hunyadi, A., & Matesz, C. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.09.080 · Cited by 12
Gaál, B., Rácz, É., Juhász, T., Holló, K., & Matesz, C. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.10.080 · Cited by 13
McDonald, A. J., Hamilton, P. G., & Barnstable, C. J. (2018) · Brain Structure and Function · doi:10.1007/s00429-017-1542-8 · Cited by 11
Bral1: “Superglue” for the extracellular matrix in the brain white matter
Cicanic, M., Syková, E., & Vargová, L. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.01.009 · Cited by 12
Matesz, C., Gaál, B., Jóhannesson, E., Dattani, A., Magyar, Á., & Wéber, I. (2015) · Neural Regeneration Research · doi:10.4103/1673-5374.165517 · Cited by 11
Dynamic Organization of Neuronal Extracellular Matrix Revealed by HaloTag-HAPLN1
Sterin, I., Niazi, A., Kim, J. S., Park, J., & Park, S. (2024) · Journal of Neuroscience · doi:10.1523/jneurosci.0666-24.2024 · Cited by 10
Bekku, Y., & Oohashi, T. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9636-7_8 · Cited by 8
Self-citationGaál, B., Kecskés, S., Matesz, C., Birinyi, A., Hunyadi, A., & Rácz, É. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.03.056 · Cited by 8
Tau Protein Modulates Perineuronal Extracellular Matrix Expression in the TauP301L-acan Mouse Model
Schmidt, S., Holzer, M., Arendt, T., Sonntag, M., & Morawski, M. (2022) · Biomolecules · doi:10.3390/biom12040505 · Cited by 8
Axonal neurotransmitter release in the regulation of myelination
Marshall-Phelps, K. L., & Almeida, R. (2024) · Bioscience Reports · doi:10.1042/bsr20231616 · Cited by 8
Dolma, S., & Joshi, A. R. (2023) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-023-10072-z · Cited by 6
Heterogeneous expression of extracellular matrix molecules in the red nucleus of the rat
Rácz, É., Gaál, B., & Matesz, C. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.02.005 · Cited by 6
Distribution of the Extracellular Matrix in the Pararubral Area of the Rat
Szarvas, D., Gaál, B., Matesz, C., & Rácz, É. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2018.10.027 · Cited by 5
Chondroitin Sulphate Proteoglycan Axonal Coats in the Human Mediodorsal Thalamic Nucleus
Pantazopoulos, H., Hossain, N. M., Chelini, G., Durning, P. T., Barbas, H., Zikopoulos, B., & Berretta, S. (2022) · Frontiers in Integrative Neuroscience · doi:10.3389/fnint.2022.934764 · Cited by 5
Nanofibers in a hyaluronan-based pericellular matrix
Gerlach, D., Kaminski, T., Pérez‐Willard, F., Kirfel, G., Gieselmann, V., & Kappler, J. (2010) · Matrix Biology · doi:10.1016/j.matbio.2010.08.006 · Cited by 4
Recombinant lectin Gg for brain imaging of glycan structure and formation in the CNS node of Ranvier
Tulin, E. K. C., Yoshimura, T., Nakazawa, C., Saito, S., Kanai, K., Kozono, T., Nakakita, S., Tonozuka, T., Ikenaka, K., & Nishikawa, A. (2022) · Journal of Neurochemistry · doi:10.1111/jnc.15695 · Cited by 3
Axon Initial Segment: Structure, Biological Functions, Diseases, and Therapeutic Targets
Song, D., Yuan, L., Yang, W., Li, W., & Li, J. (2026) · MedComm · doi:10.1002/mco2.70689 · Cited by 2
Structure and Function of Myelinated Axons
Buffington, S. A., & Rasband, M. N. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-397265-1.00078-2 · Cited by 2
Das, B., Baruah, S. M. B., Roy, S., & Bhattacharyya, D. K. (2025) · Journal of Biological Physics · doi:10.1007/s10867-025-09689-3 · Cited by 1
Chondroitin Sulfate Proteoglycans in CNS Development and Pathophysiology
Hosseini, S. M., & Karimi‐Abdolrezaee, S. (2026) · Journal of Neuroscience Research · doi:10.1002/jnr.70115 · Cited by 1
Proteoglycans of the Central Nervous System
Gupta, G. (2012) · Springer eBooks · doi:10.1007/978-3-7091-1065-2_38 · Cited by 1
Generation of brevican knockout mice
Han, X. K., & Yan, D. O. N. G. (2011) · Academic Journal of Second Military Medical University · doi:10.3724/sp.j.1008.2011.00818 · Cited by 1
The Role of Perineuronal Nets in Regulating Barrel Cortex Physiology
Chu, P. (2015) · CUNY Academic Works (City University of New York) · Cited by 1
Arab, T., Huang, Y., Nagaraj, R., Gizzie, E. A., Redding‐Ochoa, J., Troncoso, J. C., Pletniková, O., Boronina, T. N., Cole, R. N., Mahairaki, V., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.17.512628 · Cited by 1
Ayubcha, C., Dennis, E., Bhattacharyya, U., John, J., Lam, M., Lencz, T., Ge, T., & Chen, C. (2026) · medRxiv · doi:10.64898/2026.07.13.26358006 · Cited by 1
Hunanyan, A. S., García‐Alías, G., Levine, J. M., Fawcett, J. W., Mendell, L. M., & Arvanian, V. L. (2009) · Nature Precedings · doi:10.1038/npre.2009.3681.1 · Cited by 1
A Role for Focal Adhesions and Extracellular Matrix in Traumatic Axonal Injury
Hemphill, M. A. (2014) · Digital Access to Scholarship at Harvard (DASH) (Harvard University)
Molecular characterization of carnitine palmitoyltransferase 1C
Gratacòs‐Batlle, E. (2010) · Dipòsit Digital de la Universitat de Barcelona (Universitat de Barcelona)
Organizer, & Senoo, H. (2010) · Connective Tissue Research · doi:10.3109/03008207.2010.531333
Perinodal ECM - its role in diffusion barrier formation and conduction velocity in the CNS
Bekku, Y., Ninomiya, Y., & Oohashi, T. (2012) · Okayama Igakkai Zasshi (Journal of Okayama Medical Association) · doi:10.4044/joma.124.1
Self-citationDifferential Reactivity of Microglia in Two Mouse Models of Multiple Sclerosis
Hartley, R. K. (2016) · VCU Scholars Compass (Virginia Commonwealth University) · doi:10.25772/8pqb-mw19
Organization and function of molecular domains in myelinated neurons
Green, J. A. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/qmcn-th07
Proteoglycans of the Neural Stem Cell Niche
Roll, L., & Faissner, A. (2021) · Biology of extracellular matrix · doi:10.1007/978-3-030-73453-4_8
Yokosuka Science Festa 2009 Program and Proceedings June 4-June 7, 2009, Yokosuka, Japan
(2009) · Connective Tissue Research · doi:10.3109/03008200903185488
Structure and function of myelinated axons
Buffington, S. A., & Rasband, M. N. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-814405-3.00040-0
Das, B. K., Baruah, S. M. B., Singh, S., & Roy, S. (2024) · Journal of Electronics Electromedical Engineering and Medical Informatics · doi:10.35882/jeeemi.v6i2.394
Metadata
- Authors
- Bekku, Y., Rauch, U., Ninomiya, Y., & Oohashi, T.
- Affiliations
- Okayama University (JP)
- Lund University (SE)
- Corresponding author
- Oohashi, Toshitaka
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2009-02-09
- Volume
- 108
- Issue
- 5
- Pages
- 1266-1276
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W2015565810
- Cited by
- 104
- References
- 21
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 5 · 2023: 3 · 2022: 7 · 2021: 5 · 2020: 7 · 2019: 6 · 2018: 6 · 2017: 7 · 2016: 3 · 2015: 11 · 2014: 3 · 2013: 9 · 2012: 7
- FWCI
- 4.00
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nerve injury and regeneration
- Keywords
- brevican, nodes of Ranvier, myelinated axons, axon diameter, extracellular matrix assembly, tenascin-R, phosphacan, perineuronal nets, central nervous system
- MeSH terms
- Age Factors, Animals, Animals, Newborn, Axons, Central Nervous System, Hyaluronic Acid, Nerve Tissue Proteins, Chondroitin Sulfate Proteoglycans, Ranvier's Nodes, Mice, Knockout, Gene Expression Regulation, Developmental, Tenascin, Lectins, C-Type, Immunoprecipitation, Mice, Receptor-Like Protein Tyrosine Phosphatases, Class 5, Brevican
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review